Analysis of ubiquitin-dependent proteolysis in Caenorhabditis elegans.
Analysis of ubiquitin-dependent proteolysis in Caenorhabditis elegans.
复制标题
秀丽隐杆线虫泛素依赖性蛋白水解分析。
作者：
A. Segref;T. Hoppe
蛋白质稳态的维持是一个基本过程，包括未折叠和受损蛋白质的重折叠和降解，以实现有机体发育 (1)。在真核细胞中，泛素/蛋白酶体系统 (UPS) 通过调节蛋白质周转而成为蛋白质稳态的关键决定因素。在过去的十年中，对单细胞系统（例如酵母或组织培养细胞）的广泛研究揭示了有关 UPS 的详细机制。然而，进一步的挑战是破译泛素依赖性降解途径如何促进多细胞生物的细胞分化和发育。在本章中，我们描述了一种体内测定方法，用于研究多细胞生物秀丽隐杆线虫在发育过程中和分化组织中响应内在和环境挑战的蛋白质周转。该测定特别适合进行大规模遗传筛选，以鉴定对发育过程重要的新型蛋白水解因子和途径，并为未来研究组织或发育特异性蛋白稳态网络开辟新途径。
The maintenance of proteostasis is a fundamental process that encompasses refolding and degradation of unfolded and damaged proteins to enable organismal development (1). In eukaryotic cells, the ubiquitin/proteasome system (UPS) is a key determinant of proteostasis by regulating protein turnover. During the past decade, detailed mechanistic insight about the UPS was revealed from extensive studies in mono-cellular systems, such as yeast or tissue culture cells. However, a further challenge is to decipher how ubiquitin-dependent degradation pathways promote cellular differentiation and development of multicellular organisms. In this chapter, we describe an in vivo assay to study protein turnover during development and in differentiated tissues in response to intrinsic and environmental challenges in the multicellular organism Caenorhabditis elegans. This assay is particularly suitable to perform large-scale genetic screens for the identification of novel proteolysis factors and pathways important for developmental processes and opens new avenues for future investigation of tissue- or development-specific proteostasis networks.
影响因子：
56.9
作者：
BACHMAIR, A;FINLEY, D;VARSHAVSKY, A
通讯作者：
VARSHAVSKY, A
影响因子：
3.5
作者：
Timmons, L;Court, DL;Fire, A
通讯作者：
Fire, A